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7. Modulation of renal tubular cell function by RGS3

Author

Gruning, W., Arnould, T., Jochimsen, F., Sellin, L., Ananth, S., Kim, E., and Walz, G.

Subjects
Kidney tubules -- Physiological aspects, Epithelial cells -- Physiological aspects, G proteins -- Physiological aspects, Biological sciences
Abstract

A study was conducted to examine the spatial and temporal expression of RGS3, a member of the family of regulators of G protein signalling, during renal development. Results indicate that RGS3 prevents lysophosphatidic acid (LPA)-activated cell movements in mouse intermodullary collecting duct (mIMCD-3) cells. However, induction of RGS3 did not affect hepatocyte growth factor. Furthermore, it was observed that RGS3 regulates the tubular functions during renal development and in the adult kidney.

Published
1999

14. CKD-MBD

Author

Brandenburg, V.M., primary, Fliser, D., additional, Floege, J., additional, Geiger, H., additional, Hahn, K., additional, Haufe, C.C., additional, Ketteler, M., additional, Kielstein, J.T., additional, Kleophas, W., additional, Kuhlmann, M., additional, Reichel, H., additional, Sellin, L., additional, and Strutz, F., additional

Published
2013
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18. Experimental pathology

Author

McCabe, K., primary, Shobeiri, N., additional, Beseau, D., additional, Adams, M., additional, Holden, R., additional, Maio, T., additional, McCabe, K., additional, Laverty, K., additional, Pang, J., additional, Jozefacki, A., additional, Salem, S., additional, Jankowski, V., additional, Passlick-Deetjen, J., additional, Peter, M., additional, Zidek, W., additional, Jankowski, J., additional, Riser, B., additional, Barreto, F., additional, Valaitis, P., additional, Cook, C., additional, White, J., additional, Drueke, T., additional, Holmes, C., additional, Massy, Z., additional, Mizobuchi, M., additional, Ogata, H., additional, Kumata, C., additional, Nakazawa, A., additional, Koiwa, F., additional, Kinugasa, E., additional, Akizawa, T., additional, Lopez, I., additional, Aguilera-Tejero, E., additional, Guerrero, F., additional, Pineda, C., additional, Raya, A. I., additional, Peralta, A., additional, Rodriguez, M., additional, Ciceri, P., additional, Volpi, E., additional, Brenna, I., additional, Brancaccio, D., additional, Cozzolino, M., additional, Bozic, M., additional, deRoij, J., additional, Parisi, E., additional, Ruiz-Ortega, M., additional, Fernandez, E., additional, Valdivielso, J. M., additional, Lee, C.-T., additional, Ng, H.-Y., additional, Tsai, Y.-C., additional, Yang, Y.-K., additional, Niwa, T., additional, Adijiang, A., additional, Shimizu, H., additional, Nishijima, F., additional, Okamoto, T., additional, Kamata, K., additional, Naito, S., additional, Aoyama, T., additional, Tazaki, H., additional, Yamanaka, N., additional, Koenigshausen, E., additional, Ohlsson, S., additional, Woznowski, M., additional, Quack, I., additional, Potthoff, S. A., additional, Rump, L. C., additional, Sellin, L., additional, Maquigussa, E., additional, Pereira, L., additional, Arnoni, C., additional, Boim, M., additional, Lee, K. W., additional, Jeong, J. Y., additional, Jang, W. I., additional, Chung, S., additional, Choi, D. E., additional, Na, K.-R., additional, Shin, Y. T., additional, Slabiak-Blaz, N., additional, Adamczak, M., additional, Ritz, E., additional, Wiecek, A., additional, Uz, E., additional, Uz, B., additional, Sahin Balcik, O., additional, Kaya, A., additional, Akdeniz, D., additional, Bavbek Ruzgaresen, N., additional, Turgut, F. H., additional, Bayrak, R., additional, Carlioglu, A., additional, Akcay, A., additional, Galichon, P., additional, Vittoz, N., additional, Cornaire, E., additional, Baugey, E., additional, Vandermeersch, S., additional, Verpont, M.-C., additional, Mesnard, L., additional, Xu-Dubois, Y.-C., additional, Hertig, A., additional, Rondeau, E., additional, Kokeny, G., additional, Fekeshazy, O., additional, Fang, L., additional, Rosivall, L., additional, Mozes, M. M., additional, Duggan, K., additional, Hodge, G., additional, Ha, H., additional, Chen, J., additional, Lee, L., additional, Tay, C., additional, Macdonald, G., additional, Wang, P. H. M., additional, Tamouza, H., additional, Chemouny, J., additional, Monsinjon, E., additional, Tiwari, M., additional, Vende, F., additional, Vrtovsnik, F., additional, Camara, N. O., additional, Benhamou, M., additional, Monteiro, R. C., additional, Moura, I. C., additional, Rigothier, C., additional, Saleem, M., additional, Ripoche, J., additional, Mathieson, P., additional, Combe, C., additional, Welsh, G., additional, Duwel, A., additional, Munoz-Felix, J. M., additional, Lopez-Novoa, J. M., additional, Martinez-Salgado, C., additional, Koutroutsos, K., additional, Kassimatis, T., additional, Nomikos, A., additional, Giannopoulou, I., additional, Papadakis, J., additional, Nakopoulou, L., additional, Nakamichi, T., additional, Mori, T., additional, Sato, T., additional, Sato, H., additional, Ito, S., additional, Neudecker, S., additional, Heilmann, M., additional, Kramer, P., additional, Wolf, I., additional, Sticht, C., additional, Schock-Kusch, D., additional, Gubhaju, L., additional, Kriz, W., additional, Bertram, J. F., additional, Schad, L. R., additional, Gretz, N., additional, Fuentes-Calvo, I., additional, Kimura, T., additional, Takabatake, Y., additional, Takahashi, A., additional, Kaimori, J.-y., additional, Matsui, I., additional, Namba, T., additional, Kitamura, H., additional, Niimura, F., additional, Matsusaka, T., additional, Soga, T., additional, Rakugi, H., additional, Isaka, Y., additional, Shin, S. J., additional, Kim, K. S., additional, Kim, W. K., additional, Rampanelli, E., additional, Teske, G., additional, Leemans, J., additional, Florquin, S., additional, Small, D., additional, Bennett, N., additional, Roy, S., additional, Gobe, G., additional, Blazquez-Medela, A. M., additional, Garcia-Sanchez, O., additional, Lopez-Hernandez, F. J., additional, Deibel, A., additional, Cheng, J., additional, Warner, G., additional, Knudsen, B., additional, Gray, C., additional, Lien, K., additional, Juskewitch, J., additional, Grande, J., additional, Wang, N., additional, Wang, X., additional, Zeng, M., additional, Sun, B., additional, Xing, C., additional, Zhao, X., additional, Xiong, M., additional, Yang, J., additional, Cao, K., additional, Priante, G., additional, Musacchio, E., additional, Sartori, L., additional, Valvason, C., additional, Baggio, B., additional, Pitlovanciv, E. d. O. N., additional, Reis, L. A., additional, Pessoa, E. A., additional, Teixeira, L., additional, Borges, F. T., additional, Simoes, M. J., additional, Schor, N., additional, Doustar, Y., additional, Mohajeri, D., additional, Smirnov, A. V., additional, Kucher, A. G., additional, Ivanova, G. T., additional, Berseneva, O. N., additional, Parastaeva, M. M., additional, Zarajsky, M. I., additional, Saburova, I. J., additional, Kaukov, I. G., additional, Koppe, L., additional, Fouque, D., additional, Dugenet, Y., additional, Soulage, C., additional, Wan, J., additional, Yang, X., additional, Cui, J., additional, and Zou, Z., additional

Published
2011
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21. Cell signalling / Growth factors

Author

Koenigshausen, E., primary, Ruetze, M., additional, Zierhut, U., additional, Potthoff, S. A., additional, Woznowski, M., additional, Stegbauer, J., additional, Quack, I., additional, Rump, L. C., additional, Sellin, L., additional, Worthmann, K., additional, Leitges, M., additional, Dittrich-Breiholz, O., additional, Kracht, M., additional, Haller, H., additional, Schiffer, M., additional, Koenigshausen, E., additional, Grabowski, S., additional, Gerbaulet, L., additional, Kabbany, S., additional, Kramann, R., additional, Schneider, R., additional, Couson, S., additional, Kunter, U., additional, Floege, J., additional, Gigante, M., additional, De Martino, M., additional, Cormio, L., additional, Prattichizzo, C., additional, Cavalcanti, E., additional, Netti, G. S., additional, Montemurno, E., additional, Mancini, V., additional, Battaglia, M., additional, Gesualdo, L., additional, Carrieri, G., additional, and Ranieri, E., additional

Published
2011
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38. Tetrahydroaminoacridine (tacrine) stimulates neurosecretion at mammalian motor endplates

Author

Thesleff, S, Sellin, L C, Tågerud, Sven, Thesleff, S, Sellin, L C, and Tågerud, Sven

Abstract

1. Tacrine (20 microM) induced, like 4-aminoquinoline (4-AQ, 200 microM), the appearance of a population of miniature endplate potentials (m.e.p.ps) with more than twice the normal amplitude or time-to-peak. The times-to-peak of nerve impulse-evoked endplate potentials were not similarly affected. 2. Cholinesterase inhibition by edrophonium (25 microM) did not prevent tacrine or 4-AQ from inducing this population of m.e.p.ps. 3. Nerve-muscle preparations in which the normal calcium-sensitive quantal release of acetylcholine had been blocked by botulinum neurotoxin type A also responded to tacrine by an increase in the frequency of giant or slow m.e.p.ps. 4. Reduction of the temperature from 30 degrees to 14 degrees C reduced the frequency of giant or slow m.e.p.ps induced either by tacrine or by 4-AQ. A similar effect was obtained by colchicine (5 mM). This supports the idea that proximo-distal axonal transport is required for the secretory activity. 5. The neurosecretion evoked by tacrine could explain the therapeutic effects of the drug claimed in the treatment of Alzheimer's type of dementia.

Published
1990

40. Length-weight relationship and seasonal effects of the Summer Monsoon on condition factor of Terapon jarbua (Forsskål, 1775) from the wider Gulf of Aden including Socotra Island.

Author

Lavergne, E., Zajonz, U., and Sellin, L.

Subjects
LENGTH measurement, WEIGHT (Physics), TERAPONIDAE, ECONOMIC seasonal variations
Abstract

The present study investigates the length-weight relationship and condition factor of populations of the Indo-Pacific fish Terapon jarbua (Forsskål, 1775) collected in the wider Gulf of Aden, notably from Socotra Island and the Hadramout coast of Yemen. This region displays a monsoon climate, with wide seasonal variations affecting estuarine habitats. A total of 620 specimens collected in estuaries and at sea were measured and weighed during field surveys carried out in 2007 and 2008 during pre- and post- South-Western monsoon periods. The length-weight relationship of the studied populations of Terapon jarbua was determined as W = 0.0288 × SL2.99, with r 2 = 0.96 and consistent with existing data on the species from other regions. Significant seasonal differences were found in Fulton's condition factor of Terapon jarbua. [ABSTRACT FROM AUTHOR]

Published
2013
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43. Effect of Ethanol on Motor Performance and Hippocampal Population Spikes in Some Standard and Selectively Outbred Rat Strains.

Author

Sellin, L. C. and Laakso, P. S.

Abstract

Ethanol sensitivity of Wistar and Long-Evans rats was compared in vivo and in vitro. Ethanol was more effective in reducing motor performance in Long-Evans than in Wistar rats, as determined by the tilting plane test. In addition, ethanol produced a greater reduction in the population spikes recorded from hippocampal slices (in vitro) of Long-Evans rats compared to Wistar rats. When rats from the Wistar, Long-Evans, and Sprague-Dawley strains were crossbred and then selectively outbred for high (ANT) and low (AT) sensitivity to ethanol-induced impairment of motor performance, no differences were observed in the ethanol sensitivity of the hippocampal population spike between these two strains. These data suggest that differences in ethanol sensitivity may exist among standard laboratory rodent strains. Selective outbreeding may reduce or eliminate the differences in ethanol sensitivity of brain regions or neurons other than those directly involved in producing the selected behavior. Therefore, it may be incorrect to assume a general difference in ethanol sensitivity when these traits are not coselected during out-breeding, thus indicating different neuronal pools in terms of sensitivity to ethanol. [ABSTRACT FROM AUTHOR]

Published
1987
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45. 14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity.

Author

Benzing, T, Yaffe, M B, Arnould, T, Sellin, L, Schermer, B, Schilling, B, Schreiber, R, Kunzelmann, K, Leparc, G G, Kim, E, and Walz, G

Abstract

Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins (GAPs) that stimulate the inactivation of heterotrimeric G proteins. We have recently shown that RGS proteins may be regulated on a post-translational level (Benzing, T., Brandes, R., Sellin, L., Schermer, B., Lecker, S., Walz, G., and Kim, E. (1999) Nat. Med. 5, 913-918). However, mechanisms controlling the GAP activity of RGS proteins are poorly understood. Here we show that 14-3-3 proteins associate with RGS7 and RGS3. Binding of 14-3-3 is mediated by a conserved phosphoserine located in the Galpha-interacting portion of the RGS domain; interaction with 14-3-3 inhibits the GAP activity of RGS7, depends upon phosphorylation of a conserved residue within the RGS domain, and results in inhibition of GAP function. Collectively, these data indicate that phosphorylation-dependent binding of 14-3-3 may act as molecular switch that controls the GAP activity keeping a substantial fraction of RGS proteins in a dormant state.

Published
2000
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47. The polycystic kidney disease 1 gene product modulates Wnt signaling.

Author

Kim, E, Arnould, T, Sellin, L K, Benzing, T, Fan, M J, Grüning, W, Sokol, S Y, Drummond, I, and Walz, G

Abstract

Two distinct signaling pathways, involving Wnt signaling and polycystin, have been found to be critical for normal kidney development. Renal tubulogenesis requires the presence of certain Wnt proteins, whereas mutations in polycystin impede the terminal differentiation of renal tubular epithelial cells, causing the development of large cystic kidneys that characterize autosomal dominant polycystic kidney disease. Polycystin is an integral membrane protein, consisting of several extracellular motifs indicative of cell-cell and cell-matrix interactions, coupled through multiple transmembrane domains to a functionally active cytoplasmic domain. We report here that expression of the C-terminal cytoplasmic domain of polycystin stabilizes soluble endogenous beta-catenin and stimulates TCF-dependent gene transcription in human embryonic kidney cells. Microinjection of the polycystin C-terminal cytoplasmic domain induces dorsalization in zebrafish. Our findings suggest that polycystin has the capacity to modulate Wnt signaling during renal development.

Published
1999

48. Pre‐ and post‐synaptic actions of botulinum toxin at the rat neuromuscular junction.

Author

Sellin, L C and Thesleff, S

Abstract

1. Extensor digitorum longus muscles of rats were paralysed with local, non‐lethal doses of botulinum toxin Type A (BoTx). At 2 and 7 days after toxin injection, the nerve‐muscle preparations were excised and end‐plate currents analysed at 23 degrees C by dual‐micro‐electrode voltage clamp. 2. At 2 days after BoTx injection, the growth time of miniature end‐plate currents (m.e.p.c.s) increased from a rather narrow range with a mean of 0.59 to a mean of 1.35 ms with a large variability between m.e.p.c.s. End‐plate currents (e.p.c.s) were reduced compared to unpoisoned muscle. The decay phase of m.e.p.c.s and e.p.c.s, the growth phase of e.p.c.s and the voltage sensitivity of m.e.p.c.s were unchanged. 3. At 7 days after BoTx injection, the findings were similar to 2 days except that the time constant of the decay phase of m.e.p.c.s. and e.p.c.s. was about twice a long as normal and that the voltage sensitivity of m.e.p.c.s was increased. 4. The acetylcholine null potential (about 0 mV) was unchanged after treatment with BoTx. 5. The increase in the growth time of m.e.p.c.s compared to e.p.c.s following the injection of BoTx suggests that the poisoning, besides blocking quantal release, affects the time course of spontaneous but not that of evoked release. After BoTx poisoning the trans‐synaptic diffusion of a majority of spontaneously released transmitter quanta seems to occur more slowly or from areas more distant from the highest concentration of the post‐synaptic receptor than that of evoked release. 6. The increase in the decay phase of m.e.p.c.s and e.p.c.s and its increased voltage sensitivity observed in muscles poisoned for 7 days with BoTx suggest that appearance at the end‐plate of a population of new receptors with a prolonged ion channel opening time similar to that previously described for extrajunctional receptors after denervation and for junctional receptors during development.

Published
1981
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49. Acetylcholine content and release in denervated or botulinum poisoned rat skeletal muscle

Author

Polak, R. L., Sellin, L. C., and Thesleff, S.

Abstract

1. The acetylcholine (ACh) content and spontaneous and evoked release of ACh in rat extensor digitorum longus (EDL) muscles were determined by pyrolysis‐mass fragmentography. The determinations were made on muscles paralysed by local application of botulinum toxin (BoTx) type A, on unpoisoned muscles, surgically denervated or reinnervated muscles.

Published
1981
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